Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Shigella flexneri Spa15 is a chaperone of the type 3 secretion system, which binds a number of effectors to ensure their stabilization prior to secretion. One of these effectors is IpgB1, a mimic of the human Ras-like Rho guanosine triphosphatase RhoG. In this study, Spa15 alone and in complex with IpgB1 has been studied by double electron electron resonance, an experiment that gives distance information showing the spacial separation of attached spin labels. This distance is explained by determining the crystal structure of the spin-labeled Spa15 where labels are seen to be buried in hydrophobic pockets. The double electron electron resonance experiment on the Spa15 complex with IpgB1 shows that IpgB1 does not bind Spa15 in the same way as is seen in the homologous Salmonella sp. chaperone:effector complex InvB:SipA.

Original publication

DOI

10.1016/j.jmb.2010.10.053

Type

Journal article

Journal

J Mol Biol

Publication Date

14/01/2011

Volume

405

Pages

427 - 435

Keywords

Bacterial Proteins, Crystallography, X-Ray, Electron Spin Resonance Spectroscopy, Electrons, Models, Molecular, Molecular Chaperones, Protein Conformation, Shigella flexneri, Solutions, Spin Labels, rac1 GTP-Binding Protein